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10.1126/science.abf7945 http://scihub22266oqcxt.onion/10.1126/science.abf7945 33811162!8224385!33811162     free     free     free Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2021 ; 372 (6542): 642-646 Nephropedia Template TP {{tp|p=33811162|t=2021. X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease |pdf=|usr=}}{{33811162}} gab.com Text X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=33811162 #FOAvip The coronavirus disease (COVID-19) caused by SARS-CoV-2 is creating tremendous human suffering. To date, no effective drug is available to directly treat the disease. In a search for a drug against COVID-19, we have performed a high-throughput x-ray crystallographic screen of two repurposing drug libraries against the SARS-CoV-2 main protease (M(pro)), which is essential for viral replication. In contrast to commonly applied x-ray fragment screening experiments with molecules of low complexity, our screen tested already-approved drugs and drugs in clinical trials. From the three-dimensional protein structures, we identified 37 compounds that bind to M(pro) In subsequent cell-based viral reduction assays, one peptidomimetic and six nonpeptidic compounds showed antiviral activity at nontoxic concentrations. We identified two allosteric binding sites representing attractive targets for drug development against SARS-CoV-2. Twit Text FOAVip X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease ????Science http://www.kidney.de/pget.php?&tw=1&pmid=33811162 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33811162 #FOAvip English Wikipedia <ref>{{Cite pmid|33811162}}</ref> X-ray screening identifies active site and allosteric inhibitors of SARS-CoV-2 main protease #MMPMID33811162 Gunther S; Reinke PYA; Fernandez-Garcia Y; Lieske J; Lane TJ; Ginn HM; Koua FHM; Ehrt C; Ewert W; Oberthuer D; Yefanov O; Meier S; Lorenzen K; Krichel B; Kopicki JD; Gelisio L; Brehm W; Dunkel I; Seychell B; Gieseler H; Norton-Baker B; Escudero-Perez B; Domaracky M; Saouane S; Tolstikova A; White TA; Hanle A; Groessler M; Fleckenstein H; Trost F; Galchenkova M; Gevorkov Y; Li C; Awel S; Peck A; Barthelmess M; Schlunzen F; Lourdu Xavier P; Werner N; Andaleeb H; Ullah N; Falke S; Srinivasan V; Franca BA; Schwinzer M; Brognaro H; Rogers C; Melo D; Zaitseva-Doyle JJ; Knoska J; Pena-Murillo GE; Mashhour AR; Hennicke V; Fischer P; Hakanpaa J; Meyer J; Gribbon P; Ellinger B; Kuzikov M; Wolf M; Beccari AR; Bourenkov G; von Stetten D; Pompidor G; Bento I; Panneerselvam S; Karpics I; Schneider TR; Garcia-Alai MM; Niebling S; Gunther C; Schmidt C; Schubert R; Han H; Boger J; Monteiro DCF; Zhang L; Sun X; Pletzer-Zelgert J; Wollenhaupt J; Feiler CG; Weiss MS; Schulz EC; Mehrabi P; Karnicar K; Usenik A; Loboda J; Tidow H; Chari A; Hilgenfeld R; Uetrecht C; Cox R; Zaliani A; Beck T; Rarey M; Gunther S; Turk D; Hinrichs W; Chapman HN; Pearson AR; Betzel C; Meents A Science 2021[May]; 372 (6542): 642-646 PMID33811162show ga The coronavirus disease (COVID-19) caused by SARS-CoV-2 is creating tremendous human suffering. To date, no effective drug is available to directly treat the disease. In a search for a drug against COVID-19, we have performed a high-throughput x-ray crystallographic screen of two repurposing drug libraries against the SARS-CoV-2 main protease (M(pro)), which is essential for viral replication. In contrast to commonly applied x-ray fragment screening experiments with molecules of low complexity, our screen tested already-approved drugs and drugs in clinical trials. From the three-dimensional protein structures, we identified 37 compounds that bind to M(pro) In subsequent cell-based viral reduction assays, one peptidomimetic and six nonpeptidic compounds showed antiviral activity at nontoxic concentrations. We identified two allosteric binding sites representing attractive targets for drug development against SARS-CoV-2. |*Allosteric Site[MESH] |*Catalytic Domain[MESH] |*Drug Development[MESH] |Animals[MESH] |Antiviral Agents/*chemistry/pharmacology[MESH] |Chlorocebus aethiops[MESH] |Coronavirus 3C Proteases/*antagonists & inhibitors/*chemistry[MESH] |Crystallography, X-Ray[MESH] |Drug Evaluation, Preclinical[MESH] |Protease Inhibitors/*chemistry/pharmacology[MESH] |SARS-CoV-2/drug effects/*enzymology[MESH] |Vero Cells[MESH]X-ray screening identifies active site and allosteric inhibitors of SA(epmc).pdf DeepDyve Pubget Overpricing